title: Self-assembly of short collagen-related peptides into fibrils via cation-π interactions.
abstract: Introduction of a cationic residue at the N-terminus and an aromatic residue at the C-terminus of a collagen-related peptide can generate favorable cation-π interactions between the termini of collagen triple helices. The experimental results indicate that such cation-π interactions can promote the self-assembly of collagen triple helices into a higher-order structure in a head-to-tail manner. Our current work shows that cation-π interactions can serve as an effective force in preparing collagen-related biomaterials.
authors.affiliation: Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan 30013, ROC.
authors.forename: Chia-Ching
authors.initials: CC
authors.lastname: Chen
authors.forename: Wei
authors.initials: W
authors.lastname: Hsu
authors.forename: Tang-Chun
authors.initials: TC
authors.lastname: Kao
authors.forename: Jia-Cherng
authors.initials: JC
authors.lastname: Horng
mesh_terms: D000818:Animals; D040761:Biomimetic Materials / Q000737:chemistry*; D024022:Fibrillar Collagens / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D009842:Oligopeptides / Q000737:chemistry; D009994:Osmolar Concentration; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D044366:Transition Temperature
chemical_list: D024022:Fibrillar Collagens; D009842:Oligopeptides; D010455:Peptides